Journal
JOURNAL OF MOLECULAR GRAPHICS & MODELLING
Volume 22, Issue 5, Pages 451-463Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jmgm.2003.12.011
Keywords
protein folding; free energy landscape; conformation space sampling; multiple time step; P3ME
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A highly parallel replica exchange method (REM) that couples with a newly developed molecular dynamics algorithm particle-particle particle-mesh Ewald (P3ME)/RESPA has been proposed for efficient sampling of protein folding free energy landscape. The algorithm is then applied to two separate protein systems, beta-hairpin and a designed protein Trp-cage. The all-atom OPLSAA force field with an explicit solvent model is used for both protein folding simulations. Up to 64 replicas of solvated protein systems are simulated in parallel over a wide range of temperatures. The combined trajectories in temperature and configurational space allow a replica to overcome free energy barriers present at low temperatures. These large scale simulations reveal detailed results on folding mechanisms, intermediate state structures, thermodynamic properties and the temperature dependences for both protein systems. (C) 2004 Elsevier Inc. All rights reserved.
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